Evidence map›Paper›PMID 25916847›Full record

ArticleNucleic acids research2015

A prophage-encoded actin-like protein required for efficient viral DNA replication in bacteria.

Catriona Donovan, Antonia Heyer, Eugen Pfeifer, Tino Polen, Anja Wittmann, Reinhard Krämer, Julia Frunzke, Marc Bramkamp

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  9. Taxonomy, Physiology, and Natural Products of Actinobacteria.Microbiology and molecular biology reviews : MMBR · 2016
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Catriona DonovanDepartment of Biology I, Ludwig-Maximilians-University Munich, Großhaderner Str. 2-4, 82152 Planegg-Martinsried, Germany Institute for Biochemistry, University of Cologne, Zülpicherstr. 47, 50674 Cologne, Germany.
Antonia HeyerInstitut für Bio- und Geowissenschaften, IBG-1: Biotechnologie, Forschungszentrum Jülich, D-52425 Jülich, Germany.
Eugen PfeiferInstitut für Bio- und Geowissenschaften, IBG-1: Biotechnologie, Forschungszentrum Jülich, D-52425 Jülich, Germany.
Tino PolenInstitut für Bio- und Geowissenschaften, IBG-1: Biotechnologie, Forschungszentrum Jülich, D-52425 Jülich, Germany.
Anja WittmannInstitute for Biochemistry, University of Cologne, Zülpicherstr. 47, 50674 Cologne, Germany.
Reinhard KrämerInstitute for Biochemistry, University of Cologne, Zülpicherstr. 47, 50674 Cologne, Germany.
Julia FrunzkeInstitut für Bio- und Geowissenschaften, IBG-1: Biotechnologie, Forschungszentrum Jülich, D-52425 Jülich, Germany j.frunzke@fz-juelich.de.
Marc BramkampDepartment of Biology I, Ludwig-Maximilians-University Munich, Großhaderner Str. 2-4, 82152 Planegg-Martinsried, Germany Institute for Biochemistry, University of Cologne, Zülpicherstr. 47, 50674 Cologne, Germany marc.bramkamp@lmu.de.
Forschungszentrum Jülich · DEUniversity of Cologne · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In host cells, viral replication is localized at specific subcellular sites. Viruses that infect eukaryotic and prokaryotic cells often use host-derived cytoskeletal structures, such as the actin skeleton, for intracellular positioning. Here, we describe that a prophage, CGP3, integrated into the genome of Corynebacterium glutamicum encodes an actin-like protein, AlpC. Biochemical characterization confirms that AlpC is a bona fide actin-like protein and cell biological analysis shows that AlpC forms filamentous structures upon prophage induction. The co-transcribed adaptor protein, AlpA, binds to a consensus sequence in the upstream promoter region of the alpAC operon and also interacts with AlpC, thus connecting circular phage DNA to the actin-like filaments. Transcriptome analysis revealed that alpA and alpC are among the early induced genes upon excision of the CGP3 prophage. Furthermore, qPCR analysis of mutant strains revealed that both AlpA and AlpC are required for efficient phage replication. Altogether, these data emphasize that AlpAC are crucial for the spatio-temporal organization of efficient viral replication. This is remarkably similar to actin-assisted membrane localization of eukaryotic viruses that use the actin cytoskeleton to concentrate virus particles at the egress sites and provides a link of evolutionary conserved interactions between intracellular virus transport and actin.

Indexed as

DNA ReplicationVirus ReplicationActinsAdenosine TriphosphateCorynebacterium glutamicumDNA-Binding ProteinsDNA, ViralGuanosine TriphosphateProphagesViral ProteinsActinsAdenosine TriphosphateDNA-Binding ProteinsDNA, ViralGuanosine TriphosphateViral Proteins

Identifiers

PMID25916847
PMCPMC4446434
OpenAlexW2065660707

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.